The X-ray structure of a divergent cyclophilin from the nematode parasite Brugia malayi.

Abstract:

:A structure of residues 1-177 of the cyclophilin domain of a large divergent cyclophilin from the filarial nematode parasite Brugia malayi has been crystallised and solved in two different crystal forms. The active site has a similar structure to that of human cyclophilin A. Two of the 13 residues important in forming the human cyclophilin A/cyclosporin A complex are altered in the B. malayi cyclophilin and explain the relatively poor inhibition of peptidyl prolyl isomerase activity by cyclosporin A.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Taylor P,Page AP,Kontopidis G,Husi H,Walkinshaw MD

doi

10.1016/s0014-5793(98)00264-6

subject

Has Abstract

pub_date

1998-03-27 00:00:00

pages

361-6

issue

2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(98)00264-6

journal_volume

425

pub_type

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